Vicinity analysis: a methodology for the identification of similar protein active sites |
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Authors: | A. McGready A. Stevens M. Lipkin B. D. Hudson D. C. Whitley M. G. Ford |
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Affiliation: | (1) Centre for Molecular Design, Institute of Biomedical and Biomolecular Sciences, University of Portsmouth, King Henry Building, King Henry I St., Portsmouth, PO1 2DY, UK;(2) Biofocus DPI, Chesterford Research Park, Saffron Walden, Essex, CB10 1XL, UK |
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Abstract: | Vicinity analysis (VA) is a new methodology developed to identify similarities between protein binding sites based on their three-dimensional structure and the chemical similarity of matching residues. The major objective is to enable searching of the Protein Data Bank (PDB) for similar sub-pockets, especially in proteins from different structural and biochemical series. Inspection of the ligands bound in these pockets should allow ligand functionality to be identified, thus suggesting novel monomers for use in library synthesis. VA has been developed initially using the ATP binding site in kinases, an important class of protein targets involved in cell signalling and growth regulation. This paper defines the VA procedure and describes matches to the phosphate binding sub-pocket of cyclin-dependent protein kinase 2 that were found by searching a small test database that has also been used to parameterise the methodology. |
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Keywords: | Clique detection In silico protein screening Protein binding site similarity Protein kinase Receptor pocket similarity |
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